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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P04792: Variant p.Gly84Arg

Heat shock protein beta-1
Gene: HSPB1
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Variant information Variant position: help 84 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Glycine (G) to Arginine (R) at position 84 (G84R, p.Gly84Arg). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from glycine (G) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In HMND3; decreased homooligomerization; decreased heterooligomerization with HSPB6; no effect on phosphorylation by MAPKAPK2; decreased function in chaperone-mediated protein folding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 84 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 205 The length of the canonical sequence.
Location on the sequence: help ESPAVAAPAYSRALSRQLSS G VSEIRHTADRWRVSLDVNHF The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         ESPAVAA----PAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHF

                              EGPAAAAAAAAPAYSRALSRQLSSGVSEIRQTADRWRVSLD

Mouse                         EGPAAVTLAA-PAFSRALNRQLSSGVSEIRQTADRWRVSLD

Rat                           EGPAAVTLAR-PAFSRALNRQLSSGVSEIRQTADRWRVSLD

Pig                           EGPAAVAA---PAYSRLLSRQLSSGVSEIQQTADRWRVSLD

Bovine                        EG---------PAYNRALSRQLSSGVSEIQQTADRWRVSLD

Chicken                       LLPAPG-----SPYGRALS-ELSSGISEIRQSADSWKVTLD
Sequence annotation in neighborhood: help The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.
TypePositionsDescription
Chain 1 – 205 Heat shock protein beta-1
Domain 76 – 184 sHSP
Region 70 – 205 Interaction with TGFB1I1
Modified residue 65 – 65 Phosphoserine
Modified residue 78 – 78 Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5
Modified residue 82 – 82 Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5
Modified residue 83 – 83 Phosphoserine
Modified residue 86 – 86 Phosphoserine
Modified residue 98 – 98 Phosphoserine
Mutagenesis 78 – 78 S -> D. Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82.
Mutagenesis 82 – 82 S -> D. Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78.



Literature citations
Mutations in the HSP27 (HSPB1) gene cause dominant, recessive, and sporadic distal HMN/CMT type 2.
Houlden H.; Laura M.; Wavrant-De Vrieze F.; Blake J.; Wood N.; Reilly M.M.;
Neurology 71:1660-1668(2008)
Cited for: VARIANTS HMND3 LEU-39; ARG-84; MET-99; PHE-135 AND GLY-140; Structure and properties of G84R and L99M mutants of human small heat shock protein HspB1 correlating with motor neuropathy.
Nefedova V.V.; Sudnitsyna M.V.; Strelkov S.V.; Gusev N.B.;
Arch. Biochem. Biophys. 538:16-24(2013)
Cited for: CHARACTERIZATION OF VARIANTS HMND3 ARG-84 AND MET-99; INTERACTION WITH HSPB6;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.